Structure of HP1 Chromodomain Bound to a Lysine 9-Methylated Histone H3 Tail

See allHide authors and affiliations

Science  15 Mar 2002:
Vol. 295, Issue 5562, pp. 2080-2083
DOI: 10.1126/science.1069473

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


The chromodomain of the HP1 family of proteins recognizes histone tails with specifically methylated lysines. Here, we present structural, energetic, and mutational analyses of the complex between the Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9, a modification associated with epigenetic silencing. The histone tail inserts as a β strand, completing the β-sandwich architecture of the chromodomain. The methylammonium group is caged by three aromatic side chains, whereas adjacent residues form discerning contacts with one face of the chromodomain. Comparison of dimethyl- and trimethyllysine-containing complexes suggests a role for cation-π and van der Waals interactions, with trimethylation slightly improving the binding affinity.

  • * To whom correspondence should be addressed. E-mail: khorasan{at}

View Full Text

Stay Connected to Science